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61.
Ferritin, a protein widespread in nature, concentrates iron ∼1011–1012-fold above the solubility within a spherical shell of 24 subunits; it derives in plants and animals from a common ancestor
(based on sequence) but displays a cytoplasmic location in animals compared to the plastid in contemporary plants. Ferritin
gene regulation in plants and animals is altered by development, hormones, and excess iron; iron signals target DNA in plants
but mRNA in animals. Evolution has thus conserved the two end points of ferritin gene expression, the physiological signals
and the protein structure, while allowing some divergence of the genetic mechanisms. Comparison of ferritin gene organization
in plants and animals, made possible by the cloning of a dicot (soybean) ferritin gene presented here and the recent cloning
of two monocot (maize) ferritin genes, shows evolutionary divergence in ferritin gene organization between plants and animals
but conservation among plants or among animals; divergence in the genetic mechanism for iron regulation is reflected by the
absence in all three plant genes of the IRE, a highly conserved, noncoding sequence in vertebrate animal ferritin mRNA. In
plant ferritin genes, the number of introns (n= 7) is higher than in animals (n= 3). Second, no intron positions are conserved when ferritin genes of plants and animals are compared, although all ferritin
gene introns are in the coding region; within kingdoms, the intron positions in ferritin genes are conserved. Finally, secondary
protein structure has no apparent relationship to intron/exon boundaries in plant ferritin genes, whereas in animal ferritin
genes the correspondence is high. The structural differences in introns/exons among phylogenetically related ferritin coding
sequences and the high conservation of the gene structure within plant or animal kingdoms suggest that kingdom-specific functional
constraints may exist to maintain a particular intron/exon pattern within ferritin genes. In the case of plants, where ferritin
gene intron placement is unrelated to triplet codons or protein structure, and where ferritin is targeted to the plastid,
the selection pressure on gene organization may relate to RNA function and plastid/nuclear signaling.
Received: 25 July 1995 / Accepted: 3 October 1995 相似文献
62.
64.
Paul D. Roepe LiYong Wei Mary M. Hoffman Friederike Fritz 《Journal of bioenergetics and biomembranes》1996,28(6):541-555
Overexpression of the MDR protein, or p-glycoprotein (p-GP), in cells leads to decreased initial rates of accumulation and altered intracellular retention of chemotherapeutic drugs and a variety of other compounds. Thus, increased expression of the protein is related to increased drug resistance. Since several homologues of the MDR protein (CRP, ltpGPA, PDR5, sapABCDF) are also involved in conferring drug resistance phenomena in microorganisms, elucidating the function of the MDR protein at a molecular level will have important general applications. Although MDR protein function has been studied for nearly 20 years, interpretation of most data is complicated by the drug-selection conditions used to create model MDR cell lines. Precisely what level of resistance to particular drugs is conferred by a given amount of MDR protein, as well as a variety of other critical issues, are not yet resolved. Data from a number of laboratories has been gathered in support of at least four different models for the MDR protein. One model is that the protein uses the energy released from ATP hydrolysis to directly translocate drugs out of cells in some fashion. Another is that MDR protein overexpression perturbs electrical membrane potential () and/or intracellular pH (pHi) and therebyindirectly alters translocation and intracellular retention of hydrophobic drugs that are cationic, weakly basic, and/or that react with intracellular targets in a pHi, or -dependent manner. A third model proposes that the protein alternates between drug pump and Cl– channel (or channel regulator) conformations, implying that both direct and indirect mechanisms of altered drug translocation may be catalyzed by MDR protein. A fourth is that the protein acts as an ATP channel. Our recent work has tested predictions of these models via kinetic analysis of drug transport and single-cell photometry analysis of pHi, , and volume regulation in novel MDR and CFTR transfectants that have not been exposed to chemotherapeutic drugs prior to analysis. This paper reviews these data and previous work from other laboratories, as well as relevant transport physiology concepts, and summarizes how they either support or contradict the different models for MDR protein function. 相似文献
65.
生物复苏——大绝灭后生物演化历史的第一幕 总被引:12,自引:1,他引:11
生命史是一部生物界短期,快速剧变与长期,慢速稳定相互交替的历史。大绝灭(即集群绝灭)事件反映了全球环境的大突变,点断了地质历史中的生命记录及其发展历程,预示着生物界的演化出现了最有意义的飞跃,近年来尝试研究大绝灭后全球生物界的残存-复苏及其基本型式,并探索复苏的控制因素,标志着地质科学中一个重心的转移(即从大绝灭转向其后的生物残存与复苏的研究)。生物复苏揭示了大绝灭后生物演化历史的第一幕,其研究的 相似文献
66.
本文报道了中国马兜铃属12种植物的染色体数目和核型分析,发现并确定了x=8为本属染色体基数之一。本属染色体的共同特征是:小型;以中部(m),近中部(sm)着丝点染色体为主;核型类型为1A,2A,3A,1B,2B;随体一般处在染色体的长臂上。 相似文献
67.
68.
戊肝病毒活性肽的选择,合成与应用 总被引:3,自引:0,他引:3
对戊型肝炎病毒(HEV)编码蛋白序列进行了亲水性分析及二级结构预测,选择亲水性强、具有β-转角与β-折叠的区段,采用多肽固相合成法合成了HEV基因组3个开读框架(ORF1,ORF2和ORF3)中可能的抗原表位,以免疫学方法进行鉴定并选出了分别来自HEV3个ORF的、具有重要生物活性与应用前景的3段肽(EH174、EH265、EH362)。在此基础上,进行了抗HEVELISA新型检测试剂盒的实验室研究及临床试用。结果表明,所研究的戊肝抗体检测试剂盒特异性高、临床符合性好、具有可重复性,在戊肝辅助诊断及流行病学调查中具有重要意义。 相似文献
69.
草鱼出血病病毒多肽的免疫原性 总被引:10,自引:1,他引:9
采用中和试验比较了草鱼出血病病毒GCHV873的11个多肽的免疫原性,确定了主要中和抗原。纯化的单个病毒多肽免疫家兔获得抗血清,多太VP1、VP5、VP6和VP9的抗血清具有中和效价,而VP2、VP3、VP4、VP8、VP10和VP11则不能诱生中和抗体。其中VP5的抗血清中和效价最高,因此,VP6极可能是病毒多肽中的主要中和抗原。 相似文献
70.